Vis enkel innførsel

dc.contributor.authorDobrovolska, Olena
dc.contributor.authorShumilina, Elena
dc.contributor.authorGladyshev, Vadim N.
dc.contributor.authorDikiy, Alexander
dc.date.accessioned2015-10-30T14:15:34Z
dc.date.accessioned2015-11-24T14:55:00Z
dc.date.available2015-10-30T14:15:34Z
dc.date.available2015-11-24T14:55:00Z
dc.date.issued2012
dc.identifier.citationPLoS ONE 2012, 7(12)nb_NO
dc.identifier.issn1932-6203
dc.identifier.urihttp://hdl.handle.net/11250/2365569
dc.description.abstractThioredoxin glutathione reductase (TGR) is a member of the mammalian thioredoxin reductase family that has a monothiol glutaredoxin (Grx) domain attached to the thioredoxin reductase module. Here, we report a structure of the Grx domain of mouse TGR, determined through high resolution NMR spectroscopy to the final backbone RMSD value of 0.4860.10 A° . The structure represents a sandwich-like molecule composed of a four stranded b-sheet flanked by five a–helixes, with the CxxS active motif located on the catalytic loop. We structurally characterized the glutathione-binding site in the protein and describe sequence and structural relationships of the domain with glutaredoxins. The structure illuminates a key functional center that evolved in mammalian TGRs to act in thiol-disulfide reactions. Our study allows us to hypothesize that Cys105 might be functionally relevant for TGR catalysis. In addition, the data suggest that the N-terminus of Grx acts as a possible regulatory signal also protecting the protein active site from unwanted interactions in cellular cytosol.nb_NO
dc.language.isoengnb_NO
dc.publisherPublic Library of Sciencenb_NO
dc.titleStructural Analysis of Glutaredoxin Domain of Mus musculus Thioredoxin Glutathione Reductasenb_NO
dc.typeJournal articlenb_NO
dc.typePeer revieweden_GB
dc.date.updated2015-10-30T14:15:34Z
dc.source.volume7nb_NO
dc.source.journalPLoS ONEnb_NO
dc.source.issue12nb_NO
dc.identifier.doi10.1371/journal.pone.0052914
dc.identifier.cristin982336
dc.description.localcode© 2012 Dobrovolska et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.nb_NO


Tilhørende fil(er)

Thumbnail

Denne innførselen finnes i følgende samling(er)

Vis enkel innførsel